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Database: UniProt
Entry: A0A194S5M3_RHOGW
LinkDB: A0A194S5M3_RHOGW
Original site: A0A194S5M3_RHOGW 
ID   A0A194S5M3_RHOGW        Unreviewed;       396 AA.
AC   A0A194S5M3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=mRNA cap guanine-N7 methyltransferase {ECO:0000256|ARBA:ARBA00021751};
DE            EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926};
DE   AltName: Full=mRNA (guanine-N(7))-methyltransferase {ECO:0000256|ARBA:ARBA00032772};
DE   AltName: Full=mRNA cap methyltransferase {ECO:0000256|ARBA:ARBA00033387};
GN   ORFNames=RHOBADRAFT_52859 {ECO:0000313|EMBL:KPV75839.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV75839.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV75839.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV75839.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(2015).
CC   -!- FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs.
CC       {ECO:0000256|ARBA:ARBA00003378}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC         S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC         COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC         ChEBI:CHEBI:167617; EC=2.1.1.56;
CC         Evidence={ECO:0000256|ARBA:ARBA00024288};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA
CC       guanylyltransferase family. {ECO:0000256|ARBA:ARBA00008556}.
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DR   EMBL; KQ474077; KPV75839.1; -; Genomic_DNA.
DR   RefSeq; XP_018271888.1; XM_018416539.1.
DR   AlphaFoldDB; A0A194S5M3; -.
DR   STRING; 578459.A0A194S5M3; -.
DR   GeneID; 28976987; -.
DR   OMA; SHYNTLQ; -.
DR   OrthoDB; 167537at2759; -.
DR   Proteomes; UP000053890; Unassembled WGS sequence.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR   InterPro; IPR039753; RG7MT1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12189:SF2; MRNA CAP GUANINE-N7 METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR12189; MRNA GUANINE-7- METHYLTRANSFERASE; 1.
DR   Pfam; PF03291; mRNA_G-N7_MeTrfase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51562; RNA_CAP0_MT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   mRNA capping {ECO:0000256|ARBA:ARBA00023042};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00023042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          108..396
FT                   /note="MRNA cap 0 methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51562"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..79
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  44367 MW;  31692CCB03B5451E CRC64;
     MSDLHNLLES NETLKPPARP YAPIRRVTPA SSVLVPISRV ELAQCQTTVN PLRTRPKPAP
     APGAPAAAPL PPPPSSLPAR PDLALAYQQQ PQQPPAPSHK RPNTHGNGNG YGDQHDLKRW
     KGTHDTRTVA DHYNARPNTD RIARRDSPII GLKNFNNWIK SVLIAKFGRR EGDTTPRIRV
     LDLGCGKGGD LHKWTRAGTE EYVGIDIAAV SIAQAQQRYD TMRGQRFPAR FFTLDCFENP
     IEEVLPPHAV ARPFDVVSMQ FCMHYAFETE AKVRMMLANV ARYLKPGGVF VGTIPDSKNL
     FEHLSDPPDP VNSPLVFGNA VYSVKFDERE WPSPYGHRYT FFLQDAVEEV PEYVVYWDNF
     VSVAAEYGLS PVYCADFSSI FADEQEDPHF ATLLRR
//
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